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4J55

Crystal Structure of Multidrug Resistant HIV-1 Protease Clinical isolate PR20 with the potent antiviral inhibitor GRL-02031

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE 031 A 201
ChainResidue
ALEU23
AVAL82
AHOH321
BASP25
BGLY27
BALA28
BASN30
BILE32
BGLY48
BGLY49
BILE50
AASP25
BVAL82
BHOH1001
AGLY27
AALA28
AASP29
AASN30
AGLY48
AGLY49
AILE50

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 031 A 202
ChainResidue
APRO44
ALYS55
AVAL56
AGLN92
AILE93
AGLY94

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADNTIF
ChainResidueDetails
AALA22-PHE33

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
AASP25
BASP25

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APHE99
BPHE99

237423

PDB entries from 2025-06-11

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